ASTE_VIBPA
ID ASTE_VIBPA Reviewed; 342 AA.
AC Q87Q40;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Succinylglutamate desuccinylase {ECO:0000255|HAMAP-Rule:MF_00767};
DE EC=3.5.1.96 {ECO:0000255|HAMAP-Rule:MF_00767};
GN Name=astE {ECO:0000255|HAMAP-Rule:MF_00767}; OrderedLocusNames=VP1310;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH ZINC IONS.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of succinylglutamate desuccinalase from Vibrio
RT parahaemolyticus (RIMD 2210633) at the resolution 2.3 A, Northeast
RT structural genomics target Vpr14.";
RL Submitted (OCT-2005) to the PDB data bank.
CC -!- FUNCTION: Transforms N(2)-succinylglutamate into succinate and
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-L-glutamate = L-glutamate + succinate;
CC Xref=Rhea:RHEA:15169, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58763; EC=3.5.1.96;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00767};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 5/5.
CC {ECO:0000255|HAMAP-Rule:MF_00767}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate
CC desuccinylase subfamily. {ECO:0000255|HAMAP-Rule:MF_00767}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000031; BAC59573.1; -; Genomic_DNA.
DR RefSeq; NP_797689.1; NC_004603.1.
DR RefSeq; WP_005480742.1; NC_004603.1.
DR PDB; 2BCO; X-ray; 2.33 A; A/B=1-342.
DR PDBsum; 2BCO; -.
DR AlphaFoldDB; Q87Q40; -.
DR SMR; Q87Q40; -.
DR STRING; 223926.28806298; -.
DR EnsemblBacteria; BAC59573; BAC59573; BAC59573.
DR GeneID; 1188815; -.
DR KEGG; vpa:VP1310; -.
DR PATRIC; fig|223926.6.peg.1252; -.
DR eggNOG; COG2988; Bacteria.
DR HOGENOM; CLU_071608_0_0_6; -.
DR OMA; FIIAHPE; -.
DR UniPathway; UPA00185; UER00283.
DR EvolutionaryTrace; Q87Q40; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0009017; F:succinylglutamate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR CDD; cd03855; M14_ASTE; 1.
DR HAMAP; MF_00767; Arg_catab_AstE; 1.
DR InterPro; IPR007036; Aste_AspA.
DR InterPro; IPR016681; SuccinylGlu_desuccinylase.
DR Pfam; PF04952; AstE_AspA; 1.
DR PIRSF; PIRSF017020; AstE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arginine metabolism; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..342
FT /note="Succinylglutamate desuccinylase"
FT /id="PRO_0000174651"
FT ACT_SITE 219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00767"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:2BCO"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:2BCO"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:2BCO"
SQ SEQUENCE 342 AA; 38837 MW; 4FBA79C89D15D5CC CRC64;
MTKSLFRQSF LTDTLDVHID VAPAEQVLSN GVQLKLYQRG VLEVIPENPT QETKNIIISC
GIHGDETAPM ELVDSIIKDI ESGFQKVDAR CLFIIAHPES TLAHTRFLEE NLNRLFDEKE
HEPTKELAIA DTLKLLVRDF YQDTEPKTRW HLDLHCAIRG SKHYTFAVSP KTRHPVRSKA
LVDFLDSAHI EAVLLSNSPS STFSWYSAEN YSAQALTMEL GRVARIGENA LDRLTAFDLA
LRNLIAEAQP EHLSKPCIKY RVSRTIVRLH DDFDFMFDDN VENFTSFVHG EVFGHDGDKP
LMAKNDNEAI VFPNRHVAIG QRAALMVCEV KTRFEEGELV YD
